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RISS 인기검색어
- 검색키워드
- 저자 : Yingming Zhao (검색결과 5 건)
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윤태경,손요환,Yingming Zhao,노남진,강호덕 한국산림과학회 2014 Forest Science And Technology Vol.10 No.1
Intensive and continuous management has rarely been applied in forestation designed to combat desertification, except for afew instances of fertilization and irrigation in the early stage in northern China. We hypothesized that early and discontinuousfertilization and absorbent treatments would continuously increase tree growth and improve soil properties in an aridregion. In 2003 and 2004, treatments of nitrogen fertilization and absorbents were applied to Populus alba var. pyramidalistrees in an experimental windbreak site in the Hetao Plain of Inner Mongolia, China. Nevertheless, the current study resultshave demonstrated that early and discontinuous nitrogen fertilization and absorbent treatments continuously increased treegrowth (2003–2009) without any significant improvement in soil properties in 2010. The study results suggest that earlyand discontinuous fertilization and absorbent practices may be sufficiently effective in forestation aimed at combatingdesertification in arid lands where continuous maintenance cannot be expected.
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Gao, Furong,Kwon, Sung Won,Zhao, Yingming,Jin, Ying American Society for Biochemistry and Molecular Bi 2009 The Journal of biological chemistry Vol.284 No.33
<P>Transcription factors Oct4 and Sox2 are key players in maintaining the pluripotent state of embryonic stem cells (ESCs). Small changes in their levels disrupt normal expression of their target genes. However, it remains elusive how protein levels of Oct4 and Sox2 and expression of their target genes are precisely controlled in ESCs. Here we identify PARP1, a DNA-binding protein with an NAD+-dependent enzymatic activity, as a cofactor of Oct4 and Sox2 to regulate expression of their target gene FGF4. We demonstrate for the first time that PARP1 binds the FGF4 enhancer to positively regulate FGF4 expression. Our data show that PARP1 interacts with and poly(ADP-ribosyl)ates Sox2 directly, which may be a step required for dissociation and degradation of inhibitory Sox2 proteins from the FGF4 enhancer. When PARP1 activity is inhibited or absent, poly(ADP-ribosyl)ation of Sox2 decreases and association of Sox2 with FGF4 enhancers increases, accompanied by an elevated level of Sox2 proteins and reduced expression of FGF4. Significantly, specific knockdown of Sox2 expression by RNA interference can considerably abrogate the inhibitory effect of the poly(ADP-ribose) polymerase inhibitor on FGF4 expression. Interestingly, PARP1 deficiency does not affect undifferentiated ESCs but compromises cell survival and/or growth when ESCs are induced into differentiation. Addition of FGF4 can partially rescue the phenotypes caused by PARP1 deficiency during ESC differentiation. Taken together, this study uncovers new mechanisms through which Sox2 protein levels and FGF4 expression are dynamically regulated during ESC differentiation and adds a new member to the family of proteins regulating the properties of ESCs.</P>
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MS/MS of Synthetic Peptide Is Not Sufficient to Confirm New Types of Protein Modifications
Lee, Sangkyu,Tan, Minjia,Dai, Lunzhi,Kwon, Oh Kwang,Yang, Jeong Soo,Zhao, Yingming,Chen, Yue American Chemical Society 2013 JOURNAL OF PROTEOME RESEARCH Vol.12 No.2
<P>Protein post-translational modification (PTM) is one of the major regulatory mechanisms that fine-tune protein functions. Undescribed mass shifts, which may suggest novel types of PTMs, continue to be discovered because of the availabilities of more sensitive mass spectrometry technologies and more powerful sequence alignment algorithms. In this study, the histone extracted from HeLa cells was analyzed using an approach that takes advantages of in vitro propionylation, efficient peptide separation using isoelectric focusing fractionation, and the high sensitivity of the linear ion trap coupled with hybrid FT mass spectrometer. One modified peptide was identified with a new type of protein modification (+42 Da), which was assigned to acetylation of threonine 15 in histone2A. The modified peptide was verified by careful manual evaluation of the tandem mass spectrum and confirmed by high-resolution MS/MS analysis of the corresponding synthetic peptide. However, HPLC coelution and MS/MS/MS of key ions showed that the +42 Da mass shifts at threonine residue did not correspond to acetylation. The key fragment ion, y4, in the MS/MS/MS spectra (indicative of the modification site) differed between the in vivo and synthetic peptide. We showed that the misidentification was originated from sequence homologues and chemical derivitization during sample preparation. This result indicated that a more stringent procedure that includes MS/MS, MS/MS/MS, and HPLC coelution of synthetic peptides is required to identify a new PTM.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jprobs/2013/jprobs.2013.12.issue-2/pr300667e/production/images/medium/pr-2012-00667e_0005.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/pr300667e'>ACS Electronic Supporting Info</A></P>
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Li, Hui,Wang, Beibei,Yang, Acong,Lu, Rui,Wang, Weicheng,Zhou, Yang,Shi, Guilai,Kwon, Sung Won,Zhao, Yingming,Jin, Ying Wiley (John WileySons) 2009 Stem Cells Vol.27 No.6
<P>Embryonic stem cells (ESCs) possess the capacity to self-renew and differentiate into all cell types of an organism. It is essential to understand how these properties are controlled for the potential usage of their derivatives in clinical settings and reprogramming of differentiated somatic cells. Although transcriptional factors, such as Oct4, Sox2, and Nanog, have been considered as a part of the core regulatory circuitry, a growing body of evidence suggests that additional factors exist and contribute to the control of ESC self-renewal and differentiation. Here, we report that Ly-1 antibody reactive clone (LYAR), a zinc finger nucleolar protein highly expressed in undifferentiated ESCs, plays a critical role in maintaining ESC identity. Its downregulation significantly reduces the rate of ESC growth and increases their apoptosis. Moreover, reduced expression of LYAR in ESCs impairs their differentiation capacity, failing to rapidly silence pluripotency markers and to activate differentiation genes upon differentiation. Mechanistically, LYAR forms a complex with another nucleolar protein, nucleolin, and prevents its self-cleavage, maintaining a normal steady-state level of nucleolin protein in undifferentiated ESCs. Interestingly, the downregulation of nucleolin is detrimental to the growth of ESCs and increases the rate of apoptosis, similarly to the knockdown of LYAR. Thus, our data emphasize the fact that other genes besides Oct4 and Nanog are uniquely required for ESC self-renewal and differentiation and demonstrate that LYAR functions to control the stability of nucleolin protein, which in turn is essential for maintaining the self-renewal of ESCs.</P>
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